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Article

Dynamic action of the Sec machinery during initiation, protein translocation and termination.

eLife - 7 Jun 2018

Fessl Tomas, Watkins Daniel, Oatley Peter, Allen William John, Corey Robin Adam, Horne Jim, Baldwin Steve A, Radford Sheena E, Collinson Ian, Tuma Roman

Abstract excerpt

Protein translocation across cell membranes is a ubiquitous process required for protein secretion and membrane protein insertion. In bacteria, this is mostly mediated by the conserved SecYEG complex, driven through rounds of ATP hydrolysis by the cytoplasmic SecA, and the trans-membrane proton motive force. We have used single molecule techniques to explore SecY pore dynamics on multiple timescales in order to...

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Identifiers

PMID: 29877797
DOI: 10.7554/eLife.35112
PMCID: PMC6021171

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Dynamic action of the Sec machinery during initiation, protein translocation and termination.PMID 29877797Read ↗

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Unlocking the Bacterial SecY Translocon.Semantic proximity Read ↗

Critical regions of secM that control its translation and secretion and promote secretion-specific secA regulation.Semantic proximity Read ↗

Multiple SecA molecules drive protein translocation across a single translocon with SecG inversion.Semantic proximity Read ↗

SecA membrane cycling at SecYEG is driven by distinct ATP binding and hydrolysis events and is regulated by SecD and SecF.Semantic proximity Read ↗

A large conformational change couples the ATP binding site of SecA to the SecY protein channel.Semantic proximity Read ↗

Two-stage binding of SecA to the bacterial translocon regulates ribosome-translocon interaction.Semantic proximity Read ↗

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